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Literature summary extracted from

  • Singh, S.; Madzelan, P.; Stasser, J.; Weeks, C.L.; Becker, D.; Spiro, T.G.; Penner-Hahn, J.; Banerjee, R.
    Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation (2009), J. Inorg. Biochem., 103, 689-697.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 expressed as a GST-fusion protein in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 H67A mutant is comparable to wild-type, specific activity and Km values for L-Ser, L-homocysteine comparable to wild-type Homo sapiens
4.2.1.22 R266G patient mutation , mutant protein shows instability and extensive degradation during thrombin treatment. A GST-R266G fusion protein does not exhibit any detectable activity unlike the GST-tagged wild-type CBS Homo sapiens
4.2.1.22 R266K mutant is moderately pyridoxal 5'-phosphate responsive, Km value for serine is slightly elevated compared to wild-type CBS, Km value for homocysteine slightly lower compared to wild-type Homo sapiens
4.2.1.22 R266M R266M mutant shows a significantly lower basal activity, Km value for serine is slightly elevated compared to wild-type CBS, Km value for homocysteine slightly lower compared to wild-type, R266M mutant shows dramatic differences in the ferrous state. The electrostatic interaction between C52 and R266 is critical for stabilizing the ferrous heme and its disruption leads to the facile formation of a 424 nm (C-424) absorbing ferrous species, which is inactive, compared to the active 449 nm ferrous species for wild-type CBS. Resonance Raman studies on the R266M mutant reveal that the kinetics of C52 rebinding after Fe-CO photolysis are comparable to that of wild-type CBS Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.22 CO
-
Homo sapiens
4.2.1.22 HgCl2
-
Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.22 1.3
-
L-homocysteine mutant R266K Homo sapiens
4.2.1.22 1.6
-
L-homocysteine mutant R266K Homo sapiens
4.2.1.22 2
-
L-cysteine wild-type Homo sapiens
4.2.1.22 3.4
-
L-homocysteine mutant H67A Homo sapiens
4.2.1.22 4.4
-
L-cysteine mutant R266K Homo sapiens
4.2.1.22 5
-
L-homocysteine wild-type Homo sapiens
4.2.1.22 5.4
-
L-cysteine mutant H67A Homo sapiens
4.2.1.22 5.5
-
L-cysteine mutant R266K Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.22 using a glutathione sepharose column Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.22 0.68
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant R266M Homo sapiens
4.2.1.22 1.91
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant R266K Homo sapiens
4.2.1.22 2.31
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant H67A Homo sapiens
4.2.1.22 3.6
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, wild-type Homo sapiens
4.2.1.22 3.9
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant R266M Homo sapiens
4.2.1.22 5.2
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant H67A Homo sapiens
4.2.1.22 5.2
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, wild-type Homo sapiens
4.2.1.22 5.71
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant R266K Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-cysteine + L-homocysteine
-
Homo sapiens L-cystathionine + H2S
-
r

Subunits

EC Number Subunits Comment Organism
4.2.1.22 dimer
-
Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
4.2.1.22 CBS
-
Homo sapiens
4.2.1.22 cystathionine beta-synthase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.22 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.22 8.6
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 heme
-
Homo sapiens
4.2.1.22 pyridoxal 5'-phosphate
-
Homo sapiens
4.2.1.22 S-adenosyl-L-methionine
-
Homo sapiens